Beta-Filagenin, a newly identified protein coassembling with myosin and paramyosin in Caenorhabditis elegans.

ABSTRACT: Muscle thick filaments are stable assemblies of myosin and associated proteins whose dimensions are precisely regulated. The mechanisms underlying the stability and regulation of the assembly are not understood. As an approach to these problems, we have studied the core proteins that, together with paramyosin, form the core structure of the thick filament backbone in the nematode Caenorhabditis elegans. We obtained partial peptide sequences from one of the core proteins, beta-filagenin, and then identified a gene that encodes a novel protein of 201-amino acid residues from databases using these sequences. beta-Filagenin has a calculated isoelectric point at 10.61 and a high percentage of aromatic amino acids. Secondary structure algorithms predict that it consists of four beta-strands but

SUBMITTER: Liu F 

PROVIDER: S-EPMC2132574 | biostudies-literature | 1998 Jan

REPOSITORIES: biostudies-literature